Hydrogen bonding and biological specificity analysed by protein engineering

By Alan R. Fersht, Jian‐Ping Shi, J. Knill-Jones, D. M. Lowe, A. Wilkinson, D. Blow, P. Brick, P. Carter, M. Waye, G. Winter. 1985

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The protein folding problem. (2008, background): “Hydrogen bonds among backbone amide and carbonyl groups are key components of all secondary structures, and studies of mutations in different solvents estimate their strengths to be around 1–4 kcal/mol (21, 72) or stronger (5, 46).”
H++: a server for estimating pKas and adding missing hydrogens to macromolecules (2005, background): “Electrostatic interactions are often a key factor determining the properties of biomolecules (1–5), including their biological function such as catalytic activity (6,7), ligand binding (8), complex formation (9) and proton transport (10), as well as their structure and stability (11,12).”